ID A0A0L8H2X2_OCTBM Unreviewed; 2045 AA.
AC A0A0L8H2X2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
GN ORFNames=OCBIM_22023571mg {ECO:0000313|EMBL:KOF83557.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF83557.1};
RN [1] {ECO:0000313|EMBL:KOF83557.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF83557.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF83557.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ419433; KOF83557.1; -; Genomic_DNA.
DR EnsemblMetazoa; Ocbimv22023572m; Ocbimv22023572m.p; Ocbimv22023571m.g.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 3.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 3.
DR PIRSF; PIRSF039073; BRR2; 3.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 489..672
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 683..920
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1336..1511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2045 AA; 233843 MW; 638A3A5EE60842BB CRC64;
MADAAARSLQ YEYKANSNLV LQADRSLIDR RARDEATGEV ISLVGKLEGS RMGDKSKRTK
PPQMEERKVK RKKRDEAKRE VMKMKGTTLL SEGINDMVGI VYRPKTQETR QTYEVLLSFI
QAALGDQPRD VLCGAADEVL SVLKNDRMKD KERKREVESL IGSLADERFA LLVNLGKKIS
DWGSEEKMQT DENIDETYGV NVQFEESEDE DDADVFGEVR EEEEEEDEGE EAEMDATLRA
NLAEREENKK KLEGGLHPRD IDAFWLQRKL NKYYPDDPTV AQTRSKEILE ILKNAVDDRE
AENQLVMLLG VSQFEFIKIL RQHRQMVLYC TLLAQAQSAA ERKEVEEKME NDADLSNILM
ALQATEKEDI VSEQRARRHQ ARQSRMAANM EPMLANGVDQ VMSQVQLLDL DDLVFSQGSH
LMANKRCQLP DGSFRKQRKG YEEVHVPALK PKSFDQNETL IPIERLPKYA QPAFEGFKSL
NRIQSRLCKT ALETSENILL CAPTGAGKTN VALLCMLREI GKHVNNNGTI NTDEFKVVYI
APMKSLVQEM VGNFTERLKS YGLKVAELTG DHQLTKEQIT ATQVIVCTPE KWDIITRKGG
ERTYTQAVRL MIFDEIHLLH DDRGPVLESL VSRTIRNIET TREEVRLVGL SATLPNYEDI
ATFLRVDASQ GLFFFDNSYR PVPLEQQFIG ITEKKAVKRF QIMNEIVYEK VMEHAGKNQV
LVFVHSRKET GKTARAIRDM CLEKDTLGSF LKEGSASTEV LRNEAEQVKN LELRDLLPYG
FAIHHAGMTK VDRALVEDLF ADRHIQVLVS TSTLAWGVNL PAHTVIIKGT QVYSPEKGRW
VELSALDVMQ MLGRAGRPQY DTRGEGIMIT NHSELQYYLS LMNQQLPIES QFITKLADNL
NAEVVLGTVQ NMKEAINWLG YTYLYIRMLR SGPLYGVSID HQKDDPVLEQ RRKDLVHSAA
SLLDKHNLMK YDRKTGNFQV TELGRIASHF YCSHETMATY NQLLKQTLSE IELFRVFSLS
SEFKNITVRE EEKLELLKLL ERVPIPIKES IEEPSAKVNV LLQAYISQLK LEGFALMADM
VFITQSAGRL MRAIFEIVLH HGWAQLVDKA LTLCKMVDKR MWQSMSPLRQ FRKIPEEVIK
KIEKKNFPFD RLYDLNPNEI GEFIRMPKMG KTIHKYVHQF PKLELSVHIQ PITRSTLKVE
LTITPDFQWE EKVHGHSEAF WILIEDVDSE VILHHEYFLL KSKFNQDEHV VKFFVPVFEP
LPPQYFIKVI SDRWIGAETQ LPVSFRHLIL PERYPPATEL LDLQPLPVSA LRNATFEALY
SEKFPFFNPI QTQVFNAIYN SDDNVFVGAP SGSGKTICGE FAVLRMLSQN PDGRCVYVTC
LETLAQQTYT DWYNKFCLQM GKRVVLLTGE TATDLKLLAK GNIIISTPEK WDVLSRRWKQ
RKNVQSVNLF IIDELHLIGG DVGPVLEVIC SRMRYISSQL NRNIRIVALS SSLSNAKDIA
QWLGCSTGGF FNFHPNVRPV PLELHIQGFN ISHNASRIVA MSKPTYQAIL RHSTKKPVLV
FVPSRKQTRL TAIDILTFCA ADMQPNHFLH VPQTDLDPFV NKINDKTLRE TLCNGVAYLH
EGLNDTERKV IEQLFMSGAI QLVVASRNLA WGMTMTSHLV IVMDTQYYDG KAHSHLDHCL
HDHFNAEIVT KTIENKQDAV DYLTWTFLYR RMTQNPNYYN LQGVSHRHLS DHLSELVENT
INDLEQSKCI SVEDEMDVAP LNLGMIAAYY YINYTTIELF SMSLNAKTKV KGLIEIISNA
AEYESISIRH HEDQVLKQAI RLIQACVDVL SSNGWLSPAL SAMELTQMVT QAMWSKDSYL
KQLPFFTNET INRCQEKGHE TIFDIMEMED DERNALLQLS DTEMAGVARF CNRYPNIELT
FEVQDKDIIK SGSTVNVLVT LEREDEITGP VIAPFFPQKR EEGWWVVIGD SKTNSLLSIK
RLTLQQKAKV KLDFVAPSVG HHNYILFFMS DAYMGCDQEY KFSINVNKAE EEDDMSSGDN
ASDME
//
